The G2ALT gene was cloned and sequenced from the thermophilic bacterium Anoxybacillus gonensis G2. The gene is 666 bp long and encodes a protein 221 amino acids in length. The gene was overexpressed in E. coli and purified to homogeneity and biochemically characterized. The enzyme has a molecular mass of 24.5 kDa and it could be classified as a member of the family of bacterial aluminium resistance proteins based on homology searches. When this fragment was expressed in E. coli, it endowed E. coli with Al tolerance to $500{mu}M$. The purified G2ALT protein is active at a broad pH range (pH 4.0-10.0) and temperature range ($25^{circ}C-80^{circ}C$) with optima of 6.0 and the apparent optimal temperature of $73^{circ}C$ respectively. Under optimal conditions, G2ALT exhibited a low ATPase activity with $K_m-$ and $V_{max}-$ values of $10{pm}0.55{mu}M$ and $26.81{pm}0.13mg$ Pi released/min/mg enzyme, respectively. The ATPase activity of G2ALT requires $Mg^{2+}$ and $Na^+$ ions, while $Zn^{2+}$ and $Al^{3+}$ stimulate the activity. $Cd^{2+}$ and $Ag^+$ reduced the activity and $Li^+$, $Cu^{2+}$, and $Co^{2+}$ inhibited the activity. Known inhibitors of most ATPases, like such as ${eta}$-mercaptoethanol and ouabain, also inhibited the activity of the G2ALT. These biochemical characterizations suggested that G2ALT belongs to the PP-loop ATPase superfamily and it can be responsible for aluminium tolerance in A. gonensis G2.